The solution structure of a complex between the zinc-finger portion of the regulatory domain of protein kinase C (PK-C) and a small phorbol ester type ligand in the presence of lipid is continuing with specific mutants of the wild type protein. The work on the solution conformation of a cyclic hexapeptide ligand for the SH2 domain of PI3 kinase was refined and published. The effect of glycosylation on the tumor cell attachment activity of the sequence, Ser-Ile-Lys-Val-Ala-Val, from the long arm of the A chain of laminin was completed. The effect of glycosylation on other, more active sequences from the E8 domain of the alpha1 chain of laminin are currently being investigated. A systematic study of how simple carbohydrates modulate tumor cell spreading and attachment to laminin is in progress. Conformational studies including pseudorotational analysis and NOE interactions on a series of 4'-oxo- and 4'-thio- fluorinated dideoxynucleosides, are near completion. Conformational studies of cyclopropyl nucleoside derivatives and tyrosyl phosphate mimetics were completed.